(Q31080748)

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Novel protein-protein interactions of the Yersinia pestis type III secretion system elucidated with a matrix analysis by surface plasmon resonance and mass spectrometry

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scholarly article

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Europe PubMed Central

PubMed publication ID

28 June 2017

Novel protein-protein interactions of the Yersinia pestis type III secretion system elucidated with a matrix analysis by surface plasmon resonance and mass spectrometry (English)

1 reference

Europe PubMed Central

PubMed publication ID

28 June 2017

Yersinia pestis

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surface plasmon resonance

1 reference

based on heuristic

inferred from title

protein-protein interaction

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based on heuristic

inferred from title

author name string

Wieslaw Swietnicki

1

1 reference

Europe PubMed Central

PubMed publication ID

28 June 2017

Sarah O'Brien

2

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Europe PubMed Central

PubMed publication ID

28 June 2017

Kari Holman

3

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Europe PubMed Central

PubMed publication ID

28 June 2017

Scott Cherry

4

1 reference

Europe PubMed Central

PubMed publication ID

28 June 2017

Ernst Brueggemann

5

1 reference

Europe PubMed Central

PubMed publication ID

28 June 2017

Joseph E Tropea

6

1 reference

Europe PubMed Central

PubMed publication ID

28 June 2017

Harry B Hines

7

1 reference

Europe PubMed Central

PubMed publication ID

28 June 2017

David S Waugh

8

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Europe PubMed Central

PubMed publication ID

28 June 2017

Robert G Ulrich

9

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Europe PubMed Central

PubMed publication ID

28 June 2017

language of work or name

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publication date

22 June 2004

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Europe PubMed Central

PubMed publication ID

28 June 2017

number of pages

8

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Journal of Biological Chemistry

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Europe PubMed Central

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28 June 2017

279

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Europe PubMed Central

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28 June 2017

37

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Europe PubMed Central

PubMed publication ID

28 June 2017

38693-38700

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Europe PubMed Central

PubMed publication ID

28 June 2017

describes a project that uses

surface plasmon resonance

1 reference

based on heuristic

inferred from title

Supramolecular structure of the Salmonella typhimurium type III protein secretion system

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M405217200

21 January 2018

Yersinia type III secretion: send in the effectors

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M405217200

21 January 2018

Insertion of a Yop translocation pore into the macrophage plasma membrane by Yersinia enterocolitica: requirement for translocators YopB and YopD, but not LcrG.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M405217200

21 January 2018

Yersinia enterocolitica type III secretion-translocation system: channel formation by secreted Yops

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M405217200

21 January 2018

Tyrosine phosphate hydrolysis of host proteins by an essential Yersinia virulence determinant

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M405217200

21 January 2018

The PTPase YopH inhibits uptake of Yersinia, tyrosine phosphorylation of p130Cas and FAK, and the associated accumulation of these proteins in peripheral focal adhesions

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M405217200

21 January 2018

YopE of Yersinia, a GAP for Rho GTPases, selectively modulates Rac-dependent actin structures in endothelial cells

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M405217200

21 January 2018

The Yersinia Ser/Thr protein kinase YpkA/YopO directly interacts with the small GTPases RhoA and Rac-1.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M405217200

21 January 2018

The yersinia virulence factor YopM forms a novel protein complex with two cellular kinases

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M405217200

21 January 2018

Role of SycD, the chaperone of the Yersinia Yop translocators YopB and YopD.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M405217200

21 January 2018

Individual chaperones required for Yop secretion by Yersinia

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M405217200

21 January 2018

Three-dimensional secretion signals in chaperone-effector complexes of bacterial pathogens

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M405217200

21 January 2018

Yersinia enterocolitica type III secretion: yscM1 and yscM2 regulate yop gene expression by a posttranscriptional mechanism that targets the 5' untranslated region of yop mRNA.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M405217200

21 January 2018

Type III secretion chaperone-dependent regulation: activation of virulence genes by SicA and InvF in Salmonella typhimurium.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M405217200

21 January 2018

LcrF is the temperature-regulated activator of the yadA gene of Yersinia enterocolitica and Yersinia pseudotuberculosis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M405217200

21 January 2018

Temperature-controlled plasmid regulon associated with low calcium response in Yersinia pestis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M405217200

21 January 2018

Structure of the N-terminal domain of Yersinia pestis YopH at 2.0 A resolution

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M405217200

21 January 2018

Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M405217200

21 January 2018

LcrQ/YscM1, regulators of the Yersinia yop virulon, are injected into host cells by a chaperone-dependent mechanism.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M405217200

21 January 2018

LcrQ and SycH function together at the Ysc type III secretion system in Yersinia pestis to impose a hierarchy of secretion

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M405217200

21 January 2018

Yersinia enterocolitica type III secretion. On the role of SycE in targeting YopE into HeLa cells

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M405217200

21 January 2018

Interactions of the type III secretion pathway proteins LcrV and LcrG from Yersinia pestis are mediated by coiled-coil domains.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M405217200

21 January 2018

A study of the YopD-lcrH interaction from Yersinia pseudotuberculosis reveals a role for hydrophobic residues within the amphipathic domain of YopD.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M405217200

21 January 2018

The type III secretion chaperone LcrH co-operates with YopD to establish a negative, regulatory loop for control of Yop synthesis in Yersinia pseudotuberculosis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M405217200

21 January 2018

The cytosolic SycE and SycH chaperones of Yersinia protect the region of YopE and YopH involved in translocation across eukaryotic cell membranes

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M405217200

21 January 2018

Structure of the Yersinia type III secretory system chaperone SycE

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M405217200

21 January 2018

Identification of residues in the N-terminal domain of the Yersinia tyrosine phosphatase that are critical for substrate recognition

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M405217200

21 January 2018

TyeA, a protein involved in control of Yop release and in translocation of Yersinia Yop effectors.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M405217200

21 January 2018

Role of the Hha/YmoA family of proteins in the thermoregulation of the expression of virulence factors

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M405217200

21 January 2018

Evidence for direct protein-protein interaction between members of the enterobacterial Hha/YmoA and H-NS families of proteins

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M405217200

21 January 2018

Structure of the type III secretion and substrate-binding domain of Yersinia YopH phosphatase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M405217200

21 January 2018

YopD of Yersinia pseudotuberculosis is translocated into the cytosol of HeLa epithelial cells: evidence of a structural domain necessary for translocation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M405217200

21 January 2018

Targeting of the Yersinia pestis YopM protein into HeLa cells and intracellular trafficking to the nucleus

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M405217200

21 January 2018

Type III machines of pathogenic yersiniae secrete virulence factors into the extracellular milieu

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M405217200

21 January 2018

Yersinia pestis YscG protein is a Syc-like chaperone that directly binds yscE.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M405217200

21 January 2018

YscM1 and YscM2, two Yersinia enterocolitica proteins causing downregulation of yop transcription.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M405217200

21 January 2018

YscP, a Yersinia protein required for Yop secretion that is surface exposed, and released in low Ca2+.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M405217200

21 January 2018

Role of fraction 1 antigen of Yersinia pestis in inhibition of phagocytosis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M405217200

21 January 2018

Specific high affinity binding of human interleukin 1 beta by Caf1A usher protein of Yersinia pestis.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M405217200

21 January 2018

Targeting of Yersinia Yop proteins into the cytosol of HeLa cells: one-step translocation of YopE across bacterial and eukaryotic membranes is dependent on SycE chaperone

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M405217200

21 January 2018

Recombinant Yersinia enterocolitica YscM1 and YscM2: homodimer formation and susceptibility to thrombin cleavage

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M405217200

21 January 2018

Identifiers

10.1074/JBC.M405217200

1 reference

Europe PubMed Central

PubMed publication ID

28 June 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

28 June 2017

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